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Volumn 17, Issue 9, 2005, Pages 2439-2453

Monomethyl histone H3 lysine 4 as an epigenetic mark for silenced euchromatin in Chlamydomonas

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; CHROMOSOMES; ENZYMES; GENES; RNA;

EID: 31444441661     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.034165     Document Type: Article
Times cited : (75)

References (74)
  • 4
    • 0038601738 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression
    • Boa, S., Coert, C., and Patterton, H.G. (2003). Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression. Yeast 20, 827-835.
    • (2003) Yeast , vol.20 , pp. 827-835
    • Boa, S.1    Coert, C.2    Patterton, H.G.3
  • 6
    • 18244365850 scopus 로고    scopus 로고
    • PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator
    • Brown, S.A., Ripperger, J., Kadener, S., Fleury-Olela, F., Vilbois, F., Rosbash, M., and Schibler, U. (2005). PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator. Science 308, 693-696.
    • (2005) Science , vol.308 , pp. 693-696
    • Brown, S.A.1    Ripperger, J.2    Kadener, S.3    Fleury-Olela, F.4    Vilbois, F.5    Rosbash, M.6    Schibler, U.7
  • 7
    • 0037154013 scopus 로고    scopus 로고
    • Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism
    • Bryk, M., Briggs, S.D., Strahl, B.D., Curcio, M.J., Allis, C.D., and Winston, F. (2002). Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism. Curr. Biol. 12, 165-170.
    • (2002) Curr. Biol. , vol.12 , pp. 165-170
    • Bryk, M.1    Briggs, S.D.2    Strahl, B.D.3    Curcio, M.J.4    Allis, C.D.5    Winston, F.6
  • 8
    • 4043122576 scopus 로고    scopus 로고
    • Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10
    • Carvin, C.D., and Kladde, M.P. (2004). Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10. J. Biol. Chem. 279, 33057-33062.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33057-33062
    • Carvin, C.D.1    Kladde, M.P.2
  • 9
    • 0031153996 scopus 로고    scopus 로고
    • Epigenetic silencing of a foreign gene in nuclear transformants of Chlamydomonas
    • Cerutti, H., Johnson, A.M., Gillham, N.W., and Boynton, J.E. (1997). Epigenetic silencing of a foreign gene in nuclear transformants of Chlamydomonas. Plant Cell 9, 925-945.
    • (1997) Plant Cell , vol.9 , pp. 925-945
    • Cerutti, H.1    Johnson, A.M.2    Gillham, N.W.3    Boynton, J.E.4
  • 10
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng, X., Collins, R.E., and Zhang, X. (2005). Structural and sequence motifs of protein (histone) methylation enzymes. Annu. Rev. Biophys. Biomol. Struct. 34, 267-294.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 11
    • 14044256546 scopus 로고    scopus 로고
    • In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases
    • Collins, R.E., Tachibana, M., Tamaru, H., Smith, K.M., Jia, D., Zhang, X., Selker, E.U., Shinkai, Y., and Cheng, X. (2005). In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases. J. Biol. Chem. 280, 5563-5570.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5563-5570
    • Collins, R.E.1    Tachibana, M.2    Tamaru, H.3    Smith, K.M.4    Jia, D.5    Zhang, X.6    Selker, E.U.7    Shinkai, Y.8    Cheng, X.9
  • 12
    • 20444397430 scopus 로고    scopus 로고
    • Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
    • Dou, Y., Milne, T.A., Tackett, A.J., Smith, E.R., Fukuda, A., Wysocka, J., Allis, C.D., Chait, B.T., Hess, J.L., and Roeder, R.G. (2005). Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121, 873-885.
    • (2005) Cell , vol.121 , pp. 873-885
    • Dou, Y.1    Milne, T.A.2    Tackett, A.J.3    Smith, E.R.4    Fukuda, A.5    Wysocka, J.6    Allis, C.D.7    Chait, B.T.8    Hess, J.L.9    Roeder, R.G.10
  • 13
    • 23344438897 scopus 로고    scopus 로고
    • Global loss of Set1-mediated H3 Lys4 trimethylation is associated with silencing defects in Saccharomyces cerevisiae
    • Fingerman, I.M., Wu, C.-L., Wilson, B.D., and Briggs, S.D. (2005). Global loss of Set1-mediated H3 Lys4 trimethylation is associated with silencing defects in Saccharomyces cerevisiae. J. Biol. Chem. 280, 28761-28765.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28761-28765
    • Fingerman, I.M.1    Wu, C.-L.2    Wilson, B.D.3    Briggs, S.D.4
  • 15
    • 0038412822 scopus 로고    scopus 로고
    • The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase
    • Fuks, F., Hurd, P.J., Deplus, R., and Kouzarides, T. (2003). The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase. Nucleic Acids Res. 31, 2305-2312.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2305-2312
    • Fuks, F.1    Hurd, P.J.2    Deplus, R.3    Kouzarides, T.4
  • 16
    • 0038374526 scopus 로고    scopus 로고
    • Transcriptional elongation by RNA polymerase II and histone methylation
    • Gerber, M., and Shilatifard, A. (2003). Transcriptional elongation by RNA polymerase II and histone methylation. J. Biol. Chem. 278, 26303-26306.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26303-26306
    • Gerber, M.1    Shilatifard, A.2
  • 17
    • 0037216704 scopus 로고    scopus 로고
    • Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins
    • Goo, Y.H., et al. (2003). Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol. Cell. Biol. 23, 140-149.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 140-149
    • Goo, Y.H.1
  • 18
    • 0037115711 scopus 로고    scopus 로고
    • Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex
    • Guenther, M.G., Yu, J., Kao, G.D., Yen, T.J., and Lazar, M.A. (2002). Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Genes Dev. 16, 3130-3135.
    • (2002) Genes Dev. , vol.16 , pp. 3130-3135
    • Guenther, M.G.1    Yu, J.2    Kao, G.D.3    Yen, T.J.4    Lazar, M.A.5
  • 19
    • 10744224167 scopus 로고    scopus 로고
    • Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus
    • Hughes, C.M., et al. (2004). Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus. Mol. Cell 13, 587-597.
    • (2004) Mol. Cell , vol.13 , pp. 587-597
    • Hughes, C.M.1
  • 20
    • 0037154169 scopus 로고    scopus 로고
    • Suppressors of transcriptional transgenic silencing in Chlamydomonas are sensitive to DNA-damaging agents and reactivate transposable elements
    • Jeong, B.-r., Wu-Scharf, D., Zhang, C., and Cerutti, H. (2002). Suppressors of transcriptional transgenic silencing in Chlamydomonas are sensitive to DNA-damaging agents and reactivate transposable elements. Proc. Natl. Acad. Sci. USA 99, 1076-1081.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1076-1081
    • Jeong, B.-R.1    Wu-Scharf, D.2    Zhang, C.3    Cerutti, H.4
  • 21
    • 2442594080 scopus 로고    scopus 로고
    • The histone methyltransferase Trithorax and Ash1 prevent transcriptional silencing by Polycomb group proteins
    • Klymenko, T., and Muller, J. (2004). The histone methyltransferase Trithorax and Ash1 prevent transcriptional silencing by Polycomb group proteins. EMBO Rep. 5, 373-377.
    • (2004) EMBO Rep. , vol.5 , pp. 373-377
    • Klymenko, T.1    Muller, J.2
  • 22
    • 19344375746 scopus 로고    scopus 로고
    • A chromosomal memory triggered by Xist regulates histone methylation in X inactivation
    • Kohlmaier, A., Savarese, F., Lachner, M., Martens, J., Jenuwein, T., and Wutz, A. (2004). A chromosomal memory triggered by Xist regulates histone methylation in X inactivation. PLoS Biol 2, 991-1003.
    • (2004) PLoS Biol , vol.2 , pp. 991-1003
    • Kohlmaier, A.1    Savarese, F.2    Lachner, M.3    Martens, J.4    Jenuwein, T.5    Wutz, A.6
  • 23
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides, T. (2002). Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12, 198-209.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 25
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M., and Jenuwein, T. (2002). The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14, 286-298.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 26
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner, M., O'Sullivan, R.J., and Jenuwein, T. (2003). An epigenetic road map for histone lysine methylation. J. Cell Sci. 116, 2117-2124.
    • (2003) J. Cell Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 27
    • 1242344206 scopus 로고    scopus 로고
    • A plant dialect of the histone language
    • Loidl, P. (2004). A plant dialect of the histone language. Trends Plant Sci. 9, 84-90.
    • (2004) Trends Plant Sci. , vol.9 , pp. 84-90
    • Loidl, P.1
  • 30
    • 20444375490 scopus 로고    scopus 로고
    • Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription
    • Morillon, A., Karabetsou, N., Nair, A., and Mellor, J. (2005). Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription. Mol. Cell 18, 723-734.
    • (2005) Mol. Cell , vol.18 , pp. 723-734
    • Morillon, A.1    Karabetsou, N.2    Nair, A.3    Mellor, J.4
  • 32
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng, H.H., Robert, F., Young, R.A., and Struhl, K. (2003). Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell 11, 709-719.
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 33
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C.D., Tempst, P., and Reinberg, D. (2002). Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16, 479-489.
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 34
    • 0942279615 scopus 로고    scopus 로고
    • Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery
    • Pal-Bhadra, M., Leibovitch, B.A., Gandhi, S.G., Rao, M., Bhadra, U., Birchler, J.A., and Elgin, S.C. (2004). Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery. Science 303, 669-672.
    • (2004) Science , vol.303 , pp. 669-672
    • Pal-Bhadra, M.1    Leibovitch, B.A.2    Gandhi, S.G.3    Rao, M.4    Bhadra, U.5    Birchler, J.A.6    Elgin, S.C.7
  • 35
    • 3042750473 scopus 로고    scopus 로고
    • Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition
    • Perkins, E.J., Kee, B.L., and Ramsden, D.A. (2004). Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition. Nucleic Acids Res. 32, 1942-1947.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1942-1947
    • Perkins, E.J.1    Kee, B.L.2    Ramsden, D.A.3
  • 36
    • 15044366201 scopus 로고    scopus 로고
    • Methylation of histones: Playing memory with DNA
    • Peters, A.H.F.M., and Schubeler, D. (2005). Methylation of histones: Playing memory with DNA. Curr. Opin. Cell Biol. 17, 230-238.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 230-238
    • Peters, A.H.F.M.1    Schubeler, D.2
  • 37
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M.W. (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 39
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant, M.G., Daniel, J.A., Schieltz, D., Yates III, J.R., and Grant, P.A. (2005). Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 433, 434-438.
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 41
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects
    • Richards, E.J., and Elgin, S.C. (2002). Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects. Cell 108, 489-500.
    • (2002) Cell , vol.108 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.2
  • 42
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Seraphin, B. (1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 43
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • Roguev, A., Schaft, D., Shevchenko, A., Pijnappel, W.W., Wilm, M., Aasland, R., and Stewart, A.F. (2001). The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 20, 7137-7148.
    • (2001) EMBO J. , vol.20 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.4    Wilm, M.5    Aasland, R.6    Stewart, A.F.7
  • 44
    • 2442713404 scopus 로고    scopus 로고
    • A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Roguev, A., Shevchenko, A., Schaft, D., Thomas, H., and Stewart, A.F. (2004). A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Mol. Cell. Proteomics 3, 125-132.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 125-132
    • Roguev, A.1    Shevchenko, A.2    Schaft, D.3    Thomas, H.4    Stewart, A.F.5
  • 45
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila, J.S., Chen, M., Cerny, R., and Fromm, M.E. (2004). Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J. 38, 172-181.
    • (2004) Plant J. , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 46
    • 8444222059 scopus 로고    scopus 로고
    • Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas
    • Rohr, J., Sarkar, N., Balenger, S., Jeong, B.R., and Cerutti, H. (2004). Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas. Plant J. 40, 611-621.
    • (2004) Plant J. , vol.40 , pp. 611-621
    • Rohr, J.1    Sarkar, N.2    Balenger, S.3    Jeong, B.R.4    Cerutti, H.5
  • 47
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and Nei, M. (1987). The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 49
    • 9144253287 scopus 로고    scopus 로고
    • Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin
    • Santos-Rosa, H., Bannister, A.J., Dene, P.M., Geli, V., and Kouzarides, T. (2004). Methylation of H3 lysine 4 at euchromatin promotes Sir3p association with heterochromatin. J. Biol. Chem. 279, 47506-47507.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47506-47507
    • Santos-Rosa, H.1    Bannister, A.J.2    Dene, P.M.3    Geli, V.4    Kouzarides, T.5
  • 52
    • 13844306891 scopus 로고    scopus 로고
    • Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin hi in the response to alkylation-induced DNA damage
    • Sarkar, N., Lemaire, S., Wu-Scharf, D., Issakidis-Bourguet, E., and Cerutti, H. (2005). Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin hi in the response to alkylation-induced DNA damage. Eukaryot. Cell 4, 262-273.
    • (2005) Eukaryot. Cell , vol.4 , pp. 262-273
    • Sarkar, N.1    Lemaire, S.2    Wu-Scharf, D.3    Issakidis-Bourguet, E.4    Cerutti, H.5
  • 53
    • 17144365769 scopus 로고    scopus 로고
    • Histone trimethylation by Set1 is coordinated by the RRM, autoinhibitory, and catalytic domains
    • Schlichter, A., and Cairns, B.R. (2005). Histone trimethylation by Set1 is coordinated by the RRM, autoinhibitory, and catalytic domains. EMBO J. 24, 1222-1231.
    • (2005) EMBO J. , vol.24 , pp. 1222-1231
    • Schlichter, A.1    Cairns, B.R.2
  • 56
    • 0141613640 scopus 로고    scopus 로고
    • TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
    • Siegers, K., Bolter, B., Schwarz, J.P., Bottcher, U.M., Guha, S., and Hartl, F.U. (2003). TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J. 22, 5230-5240.
    • (2003) EMBO J. , vol.22 , pp. 5230-5240
    • Siegers, K.1    Bolter, B.2    Schwarz, J.P.3    Bottcher, U.M.4    Guha, S.5    Hartl, F.U.6
  • 57
    • 1642618325 scopus 로고    scopus 로고
    • Modulation of heat shock gene expression by the TAC1 chromatin-modifying complex
    • Smith, S.T., Petruk, S., Sedkov, Y., Cho, E., Tillib, S., Canaani, E., and Mazo, A. (2004). Modulation of heat shock gene expression by the TAC1 chromatin-modifying complex. Nat. Cell Biol. 6, 162-167.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 162-167
    • Smith, S.T.1    Petruk, S.2    Sedkov, Y.3    Cho, E.4    Tillib, S.5    Canaani, E.6    Mazo, A.7
  • 58
    • 18544383119 scopus 로고    scopus 로고
    • Plasticity of histone modifications across the invertebrate to vertebrate transition: Histone H3 lysine 4 trimethylation in heterochromatin
    • Spada, F., Vincent, M., and Thompson, E.M. (2005). Plasticity of histone modifications across the invertebrate to vertebrate transition: Histone H3 lysine 4 trimethylation in heterochromatin. Chromosome Res. 13, 57-72.
    • (2005) Chromosome Res. , vol.13 , pp. 57-72
    • Spada, F.1    Vincent, M.2    Thompson, E.M.3
  • 59
    • 14844346387 scopus 로고    scopus 로고
    • Genome-wide transcriptional analysis of flagellar regeneration in Chlamydomonas reinhardtii identifies orthologs of ciliary disease genes
    • Stole, V., Samanta, M.P., Tongprasit, W., and Marshall, W.F. (2005). Genome-wide transcriptional analysis of flagellar regeneration in Chlamydomonas reinhardtii identifies orthologs of ciliary disease genes. Proc. Natl. Acad. Sci. USA 102, 3703-3707.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3703-3707
    • Stole, V.1    Samanta, M.P.2    Tongprasit, W.3    Marshall, W.F.4
  • 60
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., and Shinkai, Y. (2002). G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16, 1779-1791.
    • (2002) Genes Dev. , vol.16 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10    Shinkai, Y.11
  • 62
    • 2442479896 scopus 로고    scopus 로고
    • DNA and histone methylation in plants
    • Tariq, M., and Paszkowski, J. (2004). DNA and histone methylation in plants. Trends Genet. 20, 244-251.
    • (2004) Trends Genet. , vol.20 , pp. 244-251
    • Tariq, M.1    Paszkowski, J.2
  • 63
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J., Higgins, D., and Gibson, T. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 64
    • 0036897852 scopus 로고    scopus 로고
    • Genome-wide histone modifications: Gaining specificity by preventing promiscuity
    • van Leeuwen, F., and Gottschling, D. (2002). Genome-wide histone modifications: Gaining specificity by preventing promiscuity. Curr. Opin. Cell Biol. 14, 756-762.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 756-762
    • Van Leeuwen, F.1    Gottschling, D.2
  • 65
    • 0032538445 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in Chlamydomonas reinhardtii
    • Waterborg, J.H. (1998). Dynamics of histone acetylation in Chlamydomonas reinhardtii. J. Biol. Chem. 273, 27602-27609.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27602-27609
    • Waterborg, J.H.1
  • 66
    • 0029379757 scopus 로고
    • Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and methylation
    • Waterborg, J.H., Robertson, A.J., Tatar, D.L., Borza, C.M., and Davie, J.R. (1995). Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and methylation. Plant Physiol. 109, 393-407.
    • (1995) Plant Physiol. , vol.109 , pp. 393-407
    • Waterborg, J.H.1    Robertson, A.J.2    Tatar, D.L.3    Borza, C.M.4    Davie, J.R.5
  • 67
    • 0037382574 scopus 로고    scopus 로고
    • Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1
    • Wysocka, J., Myers, M.P., Laherty, C.D., Eisenman, R.N., and Herr, W. (2003). Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 17, 896-911.
    • (2003) Genes Dev. , vol.17 , pp. 896-911
    • Wysocka, J.1    Myers, M.P.2    Laherty, C.D.3    Eisenman, R.N.4    Herr, W.5
  • 68
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • Wysocka, J., Swigut, T., Milne, T.A., Dou, Y., Zhang, X., Burlingame, A.L., Roeder, R.G., Brivanlou, A.H., and Allis, C.D. (2005). WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell 121, 859-872.
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5    Burlingame, A.L.6    Roeder, R.G.7    Brivanlou, A.H.8    Allis, C.D.9
  • 69
    • 0038492426 scopus 로고    scopus 로고
    • MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein
    • Xia, Z.-B., Anderson, M., Diaz, M.O., and Zeleznik-Le, N.J. (2003). MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein. Proc. Natl. Acad. Sci. USA 100, 8342-8347.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8342-8347
    • Xia, Z.-B.1    Anderson, M.2    Diaz, M.O.3    Zeleznik-Le, N.J.4
  • 70
    • 2942715029 scopus 로고    scopus 로고
    • Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression
    • Yokoyama, A., Wang, Z., Wysocka, J., Sanyal, M., Aufiero, D.J., Kitabayashi, I., Herr, W., and Cleary, M.L. (2004). Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol. Cell. Biol. 24, 5639-5649.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5639-5649
    • Yokoyama, A.1    Wang, Z.2    Wysocka, J.3    Sanyal, M.4    Aufiero, D.J.5    Kitabayashi, I.6    Herr, W.7    Cleary, M.L.8
  • 71
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman, P., Canas, B., Pappin, D., and Kouzarides, T. (2002). Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J. Biol. Chem. 277, 11621-11624.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 72
    • 0035984165 scopus 로고    scopus 로고
    • A WD40-repeat containing protein, similar to a fungal co-repressor, is required for transcriptional gene silencing in Chlamydomonas
    • Zhang, C., Wu-Scharf, D., Jeong, B.R., and Cerutti, H. (2002). A WD40-repeat containing protein, similar to a fungal co-repressor, is required for transcriptional gene silencing in Chlamydomonas. Plant J. 31, 25-36.
    • (2002) Plant J. , vol.31 , pp. 25-36
    • Zhang, C.1    Wu-Scharf, D.2    Jeong, B.R.3    Cerutti, H.4
  • 73
    • 10644260359 scopus 로고    scopus 로고
    • A mass spectrometric "Western blot" to evaluate the correlations between histone methylation and histone acetylation
    • Zhang, K., Siino, J.S., Jones, P.R., Yau, P.M., and Bradbury, E.M. (2004). A mass spectrometric "Western blot" to evaluate the correlations between histone methylation and histone acetylation. Proteomics 4, 3765-3775.
    • (2004) Proteomics , vol.4 , pp. 3765-3775
    • Zhang, K.1    Siino, J.S.2    Jones, P.R.3    Yau, P.M.4    Bradbury, E.M.5
  • 74
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • Zhang, X., Yang, Z., Khan, S.I., Horton, J.R., Tamaru, H., Selker, E.U., and Cheng, X. (2003). Structural basis for the product specificity of histone lysine methyltransferases. Mol. Cell 12, 177-185.
    • (2003) Mol. Cell , vol.12 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6    Cheng, X.7


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